Nucleic acid 3'-end recognition by the Argonaute2 PAZ domain

Nat Struct Mol Biol. 2004 Jun;11(6):576-7. doi: 10.1038/nsmb777. Epub 2004 May 23.


We describe the solution structures of the Argonaute2 PAZ domain bound to RNA and DNA oligonucleotides. The structures reveal a unique mode of single-stranded nucleic acid binding in which the two 3'-terminal nucleotides are buried in a hydrophobic cleft. We propose that the PAZ domain contributes to the specific recognition of siRNAs by providing a binding pocket for their characteristic two-nucleotide 3' overhangs.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Argonaute Proteins
  • Binding Sites
  • Drosophila Proteins / chemistry*
  • Drosophila Proteins / metabolism
  • Nuclear Magnetic Resonance, Biomolecular
  • Nucleic Acids / metabolism*
  • Protein Binding
  • Protein Conformation
  • RNA, Small Interfering / metabolism
  • RNA-Induced Silencing Complex / chemistry*
  • RNA-Induced Silencing Complex / metabolism
  • Solutions


  • AGO2 protein, Drosophila
  • Argonaute Proteins
  • Drosophila Proteins
  • Nucleic Acids
  • RNA, Small Interfering
  • RNA-Induced Silencing Complex
  • Solutions

Associated data

  • PDB/1T2R
  • PDB/1T2S